SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y672

- ALG6_HUMAN

UniProt

Q9Y672 - ALG6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase

Gene
ALG6, My046
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man9GlcNAc(2)-PP-Dol.

Catalytic activityi

Dolichyl beta-D-glucosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathwayi

GO - Molecular functioni

  1. glucosyltransferase activity Source: MGI

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein N-linked glycosylation Source: UniProtKB
  5. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC:2.4.1.267)
Alternative name(s):
Asparagine-linked glycosylation protein 6 homolog
Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene namesi
Name:ALG6
ORF Names:My046
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:23157. ALG6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421Helical; Reviewed predictionAdd
BLAST
Transmembranei115 – 13521Helical; Reviewed predictionAdd
BLAST
Transmembranei144 – 16421Helical; Reviewed predictionAdd
BLAST
Transmembranei173 – 19321Helical; Reviewed predictionAdd
BLAST
Transmembranei227 – 24721Helical; Reviewed predictionAdd
BLAST
Transmembranei298 – 31821Helical; Reviewed predictionAdd
BLAST
Transmembranei324 – 34421Helical; Reviewed predictionAdd
BLAST
Transmembranei362 – 38221Helical; Reviewed predictionAdd
BLAST
Transmembranei388 – 40821Helical; Reviewed predictionAdd
BLAST
Transmembranei438 – 45821Helical; Reviewed predictionAdd
BLAST
Transmembranei473 – 49321Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1C (CDG1C) [MIM:603147]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311Y → H in CDG1C. 2 Publications
Corresponds to variant rs35383149 [ dbSNP | Ensembl ].
VAR_022511
Natural varianti170 – 1701S → I in CDG1C. 1 Publication
VAR_022512
Natural varianti227 – 2271G → E in CDG1C. 1 Publication
VAR_022513
Natural varianti299 – 2991Missing in CDG1C. 1 Publication
VAR_013441
Natural varianti308 – 3081S → R in CDG1C. 1 Publication
VAR_022514
Natural varianti333 – 3331A → V in CDG1C. 3 Publications
VAR_013443
Natural varianti444 – 4441Missing in CDG1C. 1 Publication
VAR_022515
Natural varianti478 – 4781S → P in CDG1C. 1 Publication
VAR_013444

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi603147. phenotype.
Orphaneti79320. ALG6-CDG.
PharmGKBiPA134925619.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferasePRO_0000174156Add
BLAST

Proteomic databases

MaxQBiQ9Y672.
PaxDbiQ9Y672.
PRIDEiQ9Y672.

PTM databases

PhosphoSiteiQ9Y672.

Expressioni

Gene expression databases

ArrayExpressiQ9Y672.
BgeeiQ9Y672.
CleanExiHS_ALG6.
GenevestigatoriQ9Y672.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000360149.

Structurei

3D structure databases

ProteinModelPortaliQ9Y672.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287760.
HOGENOMiHOG000195048.
HOVERGENiHBG024331.
KOiK03848.
OrthoDBiEOG70088D.
PhylomeDBiQ9Y672.
TreeFamiTF314522.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 1 hit.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y672-1 [UniParc]FASTAAdd to Basket

« Hide

MEKWYLMTVV VLIGLTVRWT VSLNSYSGAG KPPMFGDYEA QRHWQEITFN    50
LPVKQWYFNS SDNNLQYWGL DYPPLTAYHS LLCAYVAKFI NPDWIALHTS 100
RGYESQAHKL FMRTTVLIAD LLIYIPAVVL YCCCLKEIST KKKIANALCI 150
LLYPGLILID YGHFQYNSVS LGFALWGVLG ISCDCDLLGS LAFCLAINYK 200
QMELYHALPF FCFLLGKCFK KGLKGKGFVL LVKLACIVVA SFVLCWLPFF 250
TEREQTLQVL RRLFPVDRGL FEDKVANIWC SFNVFLKIKD ILPRHIQLIM 300
SFCFTFLSLL PACIKLILQP SSKGFKFTLV SCALSFFLFS FQVHEKSILL 350
VSLPVCLVLS EIPFMSTWFL LVSTFSMLPL LLKDELLMPS VVTTMAFFIA 400
CVTSFSIFEK TSEEELQLKS FSISVRKYLP CFTFLSRIIQ YLFLISVITM 450
VLLTLMTVTL DPPQKLPDLF SVLVCFVSCL NFLFFLVYFN IIIMWDSKSG 500
RNQKKIS 507
Length:507
Mass (Da):58,181
Last modified:November 1, 1999 - v1
Checksum:i6558E0A318597D03
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311Y → H in CDG1C. 2 Publications
Corresponds to variant rs35383149 [ dbSNP | Ensembl ].
VAR_022511
Natural varianti170 – 1701S → I in CDG1C. 1 Publication
VAR_022512
Natural varianti226 – 2261K → N.
Corresponds to variant rs35604168 [ dbSNP | Ensembl ].
VAR_055493
Natural varianti227 – 2271G → E in CDG1C. 1 Publication
VAR_022513
Natural varianti299 – 2991Missing in CDG1C. 1 Publication
VAR_013441
Natural varianti304 – 3041F → S Common polymorphism; reduces the ability to rescue defective glycosylation of an alg6-deficient strain of S. cerevisiae during rapid growth; may exacerbate the clinical severity of patients with CDG1A. 5 Publications
Corresponds to variant rs4630153 [ dbSNP | Ensembl ].
VAR_013442
Natural varianti308 – 3081S → R in CDG1C. 1 Publication
VAR_022514
Natural varianti333 – 3331A → V in CDG1C. 3 Publications
VAR_013443
Natural varianti444 – 4441Missing in CDG1C. 1 Publication
VAR_022515
Natural varianti478 – 4781S → P in CDG1C. 1 Publication
VAR_013444

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111F → L in AAG43163. 1 Publication
Sequence conflicti374 – 3741T → P in AAG43163. 1 Publication
Sequence conflicti394 – 3941T → P in AAG43163. 1 Publication
Sequence conflicti457 – 4571T → A in AAG43163. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF102851 mRNA. Translation: AAD41466.1.
AF063604 mRNA. Translation: AAG43163.1.
AK022700 mRNA. Translation: BAG51104.1.
AL592218, AL049636 Genomic DNA. Translation: CAI18961.1.
AL049636, AL592218 Genomic DNA. Translation: CAI22829.1.
CH471059 Genomic DNA. Translation: EAX06571.1.
BC001253 mRNA. Translation: AAH01253.1.
CCDSiCCDS30735.1.
RefSeqiNP_037471.2. NM_013339.3.
UniGeneiHs.258501.

Genome annotation databases

EnsembliENST00000371108; ENSP00000360149; ENSG00000088035.
GeneIDi29929.
KEGGihsa:29929.
UCSCiuc021oof.1. human.

Polymorphism databases

DMDMi21263380.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF102851 mRNA. Translation: AAD41466.1 .
AF063604 mRNA. Translation: AAG43163.1 .
AK022700 mRNA. Translation: BAG51104.1 .
AL592218 , AL049636 Genomic DNA. Translation: CAI18961.1 .
AL049636 , AL592218 Genomic DNA. Translation: CAI22829.1 .
CH471059 Genomic DNA. Translation: EAX06571.1 .
BC001253 mRNA. Translation: AAH01253.1 .
CCDSi CCDS30735.1.
RefSeqi NP_037471.2. NM_013339.3.
UniGenei Hs.258501.

3D structure databases

ProteinModelPortali Q9Y672.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000360149.

Protein family/group databases

CAZyi GT57. Glycosyltransferase Family 57.

PTM databases

PhosphoSitei Q9Y672.

Polymorphism databases

DMDMi 21263380.

Proteomic databases

MaxQBi Q9Y672.
PaxDbi Q9Y672.
PRIDEi Q9Y672.

Protocols and materials databases

DNASUi 29929.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371108 ; ENSP00000360149 ; ENSG00000088035 .
GeneIDi 29929.
KEGGi hsa:29929.
UCSCi uc021oof.1. human.

Organism-specific databases

CTDi 29929.
GeneCardsi GC01P063834.
H-InvDB HIX0000661.
HGNCi HGNC:23157. ALG6.
MIMi 603147. phenotype.
604566. gene.
neXtProti NX_Q9Y672.
Orphaneti 79320. ALG6-CDG.
PharmGKBi PA134925619.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG287760.
HOGENOMi HOG000195048.
HOVERGENi HBG024331.
KOi K03848.
OrthoDBi EOG70088D.
PhylomeDBi Q9Y672.
TreeFami TF314522.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

ChiTaRSi ALG6. human.
GeneWikii ALG6.
GenomeRNAii 29929.
NextBioi 52559.
PROi Q9Y672.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y672.
Bgeei Q9Y672.
CleanExi HS_ALG6.
Genevestigatori Q9Y672.

Family and domain databases

InterProi IPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view ]
PANTHERi PTHR12413. PTHR12413. 1 hit.
Pfami PF03155. Alg6_Alg8. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic."
    Imbach T., Burda P., Kuhnert P., Wevers R.A., Aebi M., Berger E.G., Hennet T.
    Proc. Natl. Acad. Sci. U.S.A. 96:6982-6987(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CDG1C VAL-333.
  2. Mao Y.M., Xie Y., Zheng Z.H.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-304.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. "Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation."
    Westphal V., Murch S., Kim S., Srikrishna G., Winchester B., Day R., Freeze H.H.
    Am. J. Pathol. 157:1917-1925(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG1C HIS-131; ARG-308 AND VAL-333.
  8. Cited for: VARIANTS CDG1C VAL-333 AND PRO-478, VARIANT SER-304.
  9. "Analysis of multiple mutations in the hALG6 gene in a patient with congenital disorder of glycosylation Ic."
    Westphal V., Schottstaedt C., Marquardt T., Freeze H.H.
    Mol. Genet. Metab. 70:219-223(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1C ILE-299 DEL, VARIANT SER-304.
  10. "The T911C (F304S) substitution in the human ALG6 gene is a common polymorphism and not a causal mutation of CDG-Ic."
    Vuillaumier-Barrot S., Le Bizec C., Durand G., Seta N.
    J. Hum. Genet. 46:547-548(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-304.
  11. Cited for: VARIANTS CDG1C ILE-170 AND LEU-444 DEL.
  12. "DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG)."
    Schollen E., Martens K., Geuzens E., Matthijs G.
    Eur. J. Hum. Genet. 10:643-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1C GLU-227.
  13. "A frequent mild mutation in ALG6 may exacerbate the clinical severity of patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by phosphomannomutase deficiency."
    Westphal V., Kjaergaard S., Schollen E., Martens K., Gruenewald S., Schwartz M., Matthijs G., Freeze H.H.
    Hum. Mol. Genet. 11:599-604(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT SER-304.
  14. "Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic."
    Westphal V., Xiao M., Kwok P.-Y., Freeze H.H.
    Hum. Mutat. 22:420-421(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1C HIS-131.

Entry informationi

Entry nameiALG6_HUMAN
AccessioniPrimary (citable) accession number: Q9Y672
Secondary accession number(s): B3KMU2, Q5SXR9, Q9H3I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi